دورية أكاديمية
The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation.
| العنوان: | The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation. |
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| المؤلفون: | Brummer T; Deutsches Zentrum für Neurodegenerative Erkrankungen, Munich, Germany.; Neuroproteomics, School of Medicine, Klinikum Rechts der Isar, Technische Universität München, Munich, Germany., Pigoni M; Deutsches Zentrum für Neurodegenerative Erkrankungen, Munich, Germany.; Neuroproteomics, School of Medicine, Klinikum Rechts der Isar, Technische Universität München, Munich, Germany., Rossello A; Department of Pharmacy, Università di Pisa, Pisa, Italy., Wang H; Deutsches Zentrum für Neurodegenerative Erkrankungen, Munich, Germany.; School of Medicine, Hangzhou Normal University, Hangzhou, China., Noy PJ; School of Biosciences, University of Birmingham, Birmingham, United Kingdom., Tomlinson MG; School of Biosciences, University of Birmingham, Birmingham, United Kingdom., Blobel CP; Hospital for Special Surgery, Research Institute, New York, New York, USA.; Department of Medicine, Weill Cornell Medicine, New York, New York, USA.; Department of Physiology, Biophysics and Systems Biology, Weill Cornell Medicine, New York, New York, USA.; Institute for Advanced Study, Technische Universität München, Munich, Germany., Lichtenthaler SF; Deutsches Zentrum für Neurodegenerative Erkrankungen, Munich, Germany.; Neuroproteomics, School of Medicine, Klinikum Rechts der Isar, Technische Universität München, Munich, Germany.; Institute for Advanced Study, Technische Universität München, Munich, Germany.; Munich Cluster for Systems Neurology, Munich, Germany. |
| المصدر: | FASEB journal : official publication of the Federation of American Societies for Experimental Biology [FASEB J] 2018 Jul; Vol. 32 (7), pp. 3560-3573. Date of Electronic Publication: 2018 Feb 07. |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Federation of American Societies for Experimental Biology Country of Publication: United States NLM ID: 8804484 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1530-6860 (Electronic) Linking ISSN: 08926638 NLM ISO Abbreviation: FASEB J Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2020- : [Bethesda, Md.] : Hoboken, NJ : Federation of American Societies for Experimental Biology ; Wiley Original Publication: [Bethesda, Md.] : The Federation, [c1987- |
| مواضيع طبية MeSH: | Proteolysis*, ADAM10 Protein/*metabolism, Animals ; Cell Line, Tumor ; Cells, Cultured ; HEK293 Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Neurons/metabolism |
| مستخلص: | The transmembrane protein, ADAM10 (a disintegrin and metalloprotease 10), has key physiologic functions-for example, during embryonic development and in the brain. During transit through the secretory pathway, immature ADAM10 (proADAM10) is converted into its proteolytically active, mature form (mADAM10). Increasing or decreasing the abundance and/or activity of mADAM10 is considered to be a therapeutic approach for the treatment of such diseases as Alzheimer's disease and cancer. Yet biochemical detection and characterization of mADAM10 has been difficult. In contrast, proADAM10 is readily detected-for example, in immunoblots-which suggests that mADAM10 is only a fraction of total cellular ADAM10. Here, we demonstrate that mADAM10, but not proADAM10, unexpectedly undergoes rapid, time-dependent degradation upon biochemical cell lysis in different cell lines and in primary neurons, which prevents the detection of the majority of mADAM10 in immunoblots. This degradation required the catalytic activity of ADAM10, was efficiently prevented by adding active site inhibitors to the lysis buffer, and did not affect proADAM10, which suggests that ADAM10 degradation occurred in an intramolecular and autoproteolytic manner. Inhibition of postlysis autoproteolysis demonstrated efficient cellular ADAM10 maturation with higher levels of mADAM10 than proADAM10. Moreover, a cycloheximide chase experiment revealed that mADAM10 is a long-lived protein with a half-life of approximately 12 h. In summary, our study demonstrates that mADAM10 autoproteolysis must be blocked to allow for the proper detection of mADAM10, which is essential for the correct interpretation of biochemical and cellular studies of ADAM10.-Brummer, T., Pigoni, M., Rossello, A., Wang, H., Noy, P. J., Tomlinson, M. G., Blobel, C. P., Lichtenthaler, S. F. The metalloprotease ADAM10 (a disintegrin and metalloprotease 10) undergoes rapid, postlysis autocatalytic degradation. |
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| معلومات مُعتمدة: | R01 GM064750 United States GM NIGMS NIH HHS; PG/13/92/30587 United Kingdom British Heart Foundation |
| فهرسة مساهمة: | Keywords: ADAM17; Alzheimer’s; GI254023X; NrCAM; tetraspanin15 |
| المشرفين على المادة: | EC 3.4.24.81 (ADAM10 Protein) |
| تواريخ الأحداث: | Date Created: 20180213 Date Completed: 20190131 Latest Revision: 20190207 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC5998973 |
| DOI: | 10.1096/fj.201700823RR |
| PMID: | 29430990 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1530-6860 |
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| DOI: | 10.1096/fj.201700823RR |